ADP-ribosylation of pancreatic histone H1 and of other histones.
Incubation of pancreatic nuclei with high NAD concentrations resulted in increased ADP-ribosylation of histone H1. Interaction of [3H]ADP-ribosylated histone H1 with chromatin was significantly different from unmodified histone H1. The presence of a protein which is eluted at a lower salt concentration and which is ADP-ribosylated was also noticed. Pancreatic histones were isolated by column chromatography and their degree of ADP-ribosylation evaluated both by gel electrophoresis and by chromatography: histone H1 was the main acceptor while the core histones H3, H2B, and H2A were lightly labelled. Histones H1 and H1(0) have a differential binding to pancreatic chromatin and histone H1(0) is not ADP-ribosylated.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002843:Chromatin / Q000737:chemistry / Q000378:metabolism; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D010179:Pancreas / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism; D051381:Rats
D002843:Chromatin; D006657:Histones; D009702:Nucleoside Diphosphate Sugars; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases